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Browsing Biotechnology by Subject "Binding constant"

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    Biophysical Interaction of Propylthiouracil with Human and Bovine Serum Albumins
    (BMC, 2019-01-30) Alsamamra, Husain; Abuteir, Musa; Darwish, Saqer
    The physical interaction of antithyroid drug, propylthiouracil was studied with bovine and human serum albumins through UV absorption and fluorescence spectroscopic techniques. The obtained values of the quenching constants were calculated by the Stern-Volmer equation are in the order of 1012 Lmol-1 s-1 indicating that both serum albumins were quenched by the drug in a static manner. The binding constants of the drug interaction with both HSA and BSA proteins are found to be relatively weak and are in the order of 103 M-1. The tryptophan residues of HSA and BSA are most perturbed by the binding process which was authenticated by the fluorescence spectra of both proteins in the presence of propylthiouracil. The importance behind this study is to clarify the mechanism of the interaction between propylthiouracil with HSA and BSA, as well as providing additional values in order to study drug-protein interaction which may facilitate the study of drug metabolism and transportation.
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    Spectroscopic investigations of pentobarbital interaction with human serum albumin
    (Elsevier, 2010-01-29) Darwish, Saqer M.; Abu sharkh, Sawsan E.; Abu Teir, Musa M.; Makharza, Sami A.; Abu-hadid, Mahmoud M.
    The interaction between pentobarbital and human serum albumin has been investigated. The basic binding interaction was studied by UV-absorption and fluorescence spectroscopy. From spectral analysis pentobarbital showed a strong ability to quench the intrinsic fluorescence of HSA through a static quenching procedure. The binding constant (k) is estimated at 1.812 104 M 1 at 293 K. FT-IR spectroscopy with Fourier self-deconvolution technique was used to determine the protein secondary structure and drug binding mechanisms. The observed spectral changes of HSA–pentobarbital complex indicate a larger intensity decrease in the absorption band of a-helix relative to that of b-sheets. This variation in intensity is related indirectly to the formation of H-bonding in the complex molecules, which accounts for the different intrinsic propensities of a-helix and b-sheets.